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Database: UniProt/SWISS-PROT
Entry: ALR_SORC5
LinkDB: ALR_SORC5
Original site: ALR_SORC5 
ID   ALR_SORC5               Reviewed;         379 AA.
AC   A9ESU7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   07-JUN-2017, entry version 62.
DE   RecName: Full=Alanine racemase {ECO:0000255|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000255|HAMAP-Rule:MF_01201};
GN   Name=alr; OrderedLocusNames=sce7251;
OS   Sorangium cellulosum (strain So ce56) (Polyangium cellulosum (strain
OS   So ce56)).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Sorangiineae; Polyangiaceae; Sorangium.
OX   NCBI_TaxID=448385;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=So ce56;
RX   PubMed=17965706; DOI=10.1038/nbt1354;
RA   Schneiker S., Perlova O., Kaiser O., Gerth K., Alici A.,
RA   Altmeyer M.O., Bartels D., Bekel T., Beyer S., Bode E., Bode H.B.,
RA   Bolten C.J., Choudhuri J.V., Doss S., Elnakady Y.A., Frank B.,
RA   Gaigalat L., Goesmann A., Groeger C., Gross F., Jelsbak L.,
RA   Jelsbak L., Kalinowski J., Kegler C., Knauber T., Konietzny S.,
RA   Kopp M., Krause L., Krug D., Linke B., Mahmud T., Martinez-Arias R.,
RA   McHardy A.C., Merai M., Meyer F., Mormann S., Munoz-Dorado J.,
RA   Perez J., Pradella S., Rachid S., Raddatz G., Rosenau F., Rueckert C.,
RA   Sasse F., Scharfe M., Schuster S.C., Suen G., Treuner-Lange A.,
RA   Velicer G.J., Vorholter F.-J., Weissman K.J., Welch R.D., Wenzel S.C.,
RA   Whitworth D.E., Wilhelm S., Wittmann C., Bloecker H., Puehler A.,
RA   Mueller R.;
RT   "Complete genome sequence of the myxobacterium Sorangium cellulosum.";
RL   Nat. Biotechnol. 25:1281-1289(2007).
CC   -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-
CC       alanine. May also act on other amino acids. {ECO:0000255|HAMAP-
CC       Rule:MF_01201}.
CC   -!- CATALYTIC ACTIVITY: L-alanine = D-alanine. {ECO:0000255|HAMAP-
CC       Rule:MF_01201}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01201};
CC   -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-
CC       alanine from L-alanine: step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_01201}.
CC   -!- SIMILARITY: Belongs to the alanine racemase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01201}.
DR   EMBL; AM746676; CAN97420.1; -; Genomic_DNA.
DR   ProteinModelPortal; A9ESU7; -.
DR   SMR; A9ESU7; -.
DR   STRING; 448385.sce7251; -.
DR   PRIDE; A9ESU7; -.
DR   EnsemblBacteria; CAN97420; CAN97420; sce7251.
DR   KEGG; scl:sce7251; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031444; -.
DR   KO; K01775; -.
DR   OMA; WEILCGF; -.
DR   OrthoDB; POG091H022F; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000002139; Chromosome.
DR   GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030632; P:D-alanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.40.37.10; -; 1.
DR   Gene3D; 3.20.20.10; -; 1.
DR   HAMAP; MF_01201; Ala_racemase; 1.
DR   InterPro; IPR000821; Ala_racemase.
DR   InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR   InterPro; IPR011079; Ala_racemase_C.
DR   InterPro; IPR001608; Ala_racemase_N.
DR   InterPro; IPR020622; Ala_racemase_pyridoxalP-BS.
DR   InterPro; IPR029066; PLP-binding_barrel.
DR   Pfam; PF00842; Ala_racemase_C; 1.
DR   Pfam; PF01168; Ala_racemase_N; 1.
DR   PRINTS; PR00992; ALARACEMASE.
DR   SMART; SM01005; Ala_racemase_C; 1.
DR   SUPFAM; SSF50621; SSF50621; 1.
DR   SUPFAM; SSF51419; SSF51419; 1.
DR   TIGRFAMs; TIGR00492; alr; 1.
DR   PROSITE; PS00395; ALANINE_RACEMASE; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Isomerase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN         1    379       Alanine racemase.
FT                                /FTId=PRO_1000138623.
FT   ACT_SITE     37     37       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    266    266       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   BINDING     139    139       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01201}.
FT   BINDING     314    314       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   MOD_RES      37     37       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
SQ   SEQUENCE   379 AA;  40620 MW;  8A4637A0E2661C48 CRC64;
     MRPTRAEVNL AHLRHNLRVL ERGLTGATKP QIWGVLKADA YGHGAPAVAR TLERAGIPGL
     CVALLEEAIE LRDAGIRLPI LVMGGYYGPR RDGFEEIIAR DLVPVVYDAG QIERLASVVR
     LEQRGRVGVH LKVDTGMGRL GAASSEIEAV LATLAKHPEV KLDGLMTHLA CADADDLGVT
     IEQMRLFGEI EQRAKSFGLT PRVRHASNSA AMLRLPAALL DIVRPGVALF GISPCAGLAP
     DLKPVIRVRS EIVALRTIAK GDRIGYGHTW QASRESVVAT VPMGYADGLS RQLSNRGAAL
     VRGQRAPIAG AVSMDLTMLD VTDVPGARLG DEVVFLGTQD GPLGRGTISA EEIAGLTGTI
     AWEVLTSISR RVPRFYREP
//
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